Description_x000D_ General description_x000D_ Trypsin Inhibitor from Glycine max (soybean) also known as Kunitz trypsin inhibitor is a 21 kDa protein with a single trypsin binding reactive site._x000D_ Application_x000D_ Trypsin Inhibitor from Glycine max (soybean) has been used:_x000D_ • as a standard protein to measure the amount of endogenous trypsin inhibitor present in midgut lysate (M1) of Riptortus pedestris_x000D_ • as a standard to compare the trypsin inhibitory activity of the purified protein_x000D_ • to monitor the trypsin inhibitory activity by fractionating in MonoS cation exchange chromatography_x000D_ • as an trypsin inhibitor_x000D_ Packaging_x000D_ 5, 10, 25 mg in glass bottle_x000D_ Biochem/physiol Actions_x000D_ Soybean trypsin inhibitor inhibits trypsin and to a lesser extent chymotrypsin and plasmin. It forms a 1:1 stoichiometric complex with trypsin. Upon formation of this complex, trypsin may cleave a single arginine-isoleucine bond in the inhibitor. Dissociation of this complex may yield the modified form or the native inhibitor. At the optimal pH for trypsin binding (pH 8.0), the association constant is ≥ 10x108._x000D_ Trypsin Inhibitor from Glycine max (soybean) binds with the active site of trypsin enzyme, in a competitive inhibition manner._x000D_ Unit Definition_x000D_ One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path._x000D_ Preparation Note_x000D_ Further purification of T9128 yielding an electrophoretically pure Kunitz inhibitor with increased activity._x000D_ Trypsin inhibitor is soluble in water and phosphate buffers at concentrations of 10 mg/ml or higher. Solutions at higher concentrations may be hazy and have a yellow to amber color._x000D_ Analysis Note_x000D_ One mg will inhibit ≥1.0 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein._x000D_ Other Notes_x000D_ View more information on Trypsin Inhibitor.